Engineered Peptides Enable Biomimetic Route for Collagen Intrafibrillar Mineralization.

Autor: Cloyd AK; Bioengineering Program, University of Kansas, Lawrence, KS 66045, USA.; Institute for Bioengineering Research, University of Kansas, Lawrence, KS 66045, USA., Boone K; Institute for Bioengineering Research, University of Kansas, Lawrence, KS 66045, USA.; Department of Mechanical Engineering, University of Kansas, Lawrence, KS 66045, USA., Ye Q; Institute for Bioengineering Research, University of Kansas, Lawrence, KS 66045, USA., Snead ML; Center for Craniofacial Molecular Biology, Herman Ostrow School of Dentistry of USC, University of Southern California, Los Angeles, CA 90007, USA., Spencer P; Bioengineering Program, University of Kansas, Lawrence, KS 66045, USA.; Institute for Bioengineering Research, University of Kansas, Lawrence, KS 66045, USA.; Department of Mechanical Engineering, University of Kansas, Lawrence, KS 66045, USA., Tamerler C; Bioengineering Program, University of Kansas, Lawrence, KS 66045, USA.; Institute for Bioengineering Research, University of Kansas, Lawrence, KS 66045, USA.; Department of Mechanical Engineering, University of Kansas, Lawrence, KS 66045, USA.
Jazyk: angličtina
Zdroj: International journal of molecular sciences [Int J Mol Sci] 2023 Mar 28; Vol. 24 (7). Date of Electronic Publication: 2023 Mar 28.
DOI: 10.3390/ijms24076355
Abstrakt: Overcoming the short lifespan of current dental adhesives remains a significant clinical need. Adhesives rely on formation of the hybrid layer to adhere to dentin and penetrate within collagen fibrils. However, the ability of adhesives to achieve complete enclosure of demineralized collagen fibrils is recognized as currently unattainable. We developed a peptide-based approach enabling collagen intrafibrillar mineralization and tested our hypothesis on a type-I collagen-based platform. Peptide design incorporated collagen-binding and remineralization-mediating properties using the domain structure conservation approach. The structural changes from representative members of different peptide clusters were generated for each functional domain. Common signatures associated with secondary structure features and the related changes in the functional domain were investigated by attenuated total reflectance Fourier-transform infrared (ATR-FTIR) and circular dichroism (CD) spectroscopy, respectively. Assembly and remineralization properties of the peptides on the collagen platforms were studied using atomic force microscopy (AFM). Mechanical properties of the collagen fibrils remineralized by the peptide assemblies was studied using PeakForce-Quantitative Nanomechanics (PF-QNM)-AFM. The engineered peptide was demonstrated to offer a promising route for collagen intrafibrillar remineralization. This approach offers a collagen platform to develop multifunctional strategies that combine different bioactive peptides, polymerizable peptide monomers, and adhesive formulations as steps towards improving the long-term prospects of composite resins.
Databáze: MEDLINE
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